Phosphorylation-dependent binding of mitotic cyclins to Cdc6 contributes to DNA replication control

Nature

Volumn 431, Issue 7012, 2004, Pages 1118-1123

  Mimura, Satoru ^a   Seki, Takashi ^a,b   Tanaka, Seiji ^a,c   Diffley, John F X ^a  

^a IMPERIAL CANCER RESEARCH FUND   (United Kingdom)

^b NAGOYA UNIVERSITY   (Japan)

^c NATIONAL INSTITUTE OF GENETICS   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; CELLS; DNA; POLYPEPTIDES; SUBSTRATES; YEAST;

CELL CYCLE; CYCLIN-DEPENDENT KINASES (CDK); PHOSPHOPEPTIDES;

ENZYMES;

CELL CYCLE PROTEIN; CYCLIN A; CYCLIN B; CYCLIN DEPENDENT KINASE 6; CYCLIN E; CYCLINE; MINICHROMOSOME MAINTENANCE PROTEIN 2; PEPTIDE DERIVATIVE; PHOSPHOPEPTIDE; PROTEIN CDC28; PROTEIN CLB2; PROTEIN MCM7; PROTEIN ORC; PROTEIN SUBUNIT; RECOMBINANT PROTEIN; REPLICATION LICENSING FACTOR CDT1; UNCLASSIFIED DRUG; CDC6 PROTEIN, S CEREVISIAE; CELL EXTRACT; CLB2 PROTEIN, S CEREVISIAE; CYCLIN DEPENDENT KINASE 1; PEPTIDE FRAGMENT; SACCHAROMYCES CEREVISIAE PROTEIN;

BIOLOGY;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CELL CYCLE G2 PHASE; CELL CYCLE S PHASE; COMPLEX FORMATION; CONTROLLED STUDY; DNA REPLICATION; ENZYME SUBSTRATE COMPLEX; METAPHASE; MITOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; SACCHAROMYCES CEREVISIAE; BINDING SITE; CHEMISTRY; CYTOLOGY; DRUG ANTAGONISM; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; HELA CELL; HUMAN; METABOLISM; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE;

SACCHAROMYCES; SACCHAROMYCES CEREVISIAE; SACCHAROMYCETALES;

AMINO ACID MOTIFS; BINDING SITES; CDC28 PROTEIN KINASE, S CEREVISIAE; CELL CYCLE PROTEINS; CELL EXTRACTS; CYCLIN B; CYCLINS; DNA REPLICATION; HELA CELLS; HUMANS; MITOSIS; PEPTIDE FRAGMENTS; PHOSPHOPEPTIDES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SUBSTRATE SPECIFICITY;

EID: 7744234408     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature03024     Document Type: Article

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